Glucosidase Beta, Acid 3 (GbA3)

GBA3 is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides . GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism. The predicted 469-amino acid CBGL1 protein is 84% identical to the guinea pig protein. It possesses a beta-glucosidase-like domain with 2 conserved active-site glu residues that is more than 40% identical to some of the beta-glucosidase-like domains of the KL and lactase-phlorizin hydrolase (LCT) proteins. In contrast to KL, however, CBGL1 has no signal sequence or transmembrane domain, suggesting a cytoplasmic distribution.